A virulence locus of Pseudomonas 276 aeruginosa encodes a protein secretion apparatus, Science, vol.312, pp.1526-1530, 2006. ,
Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin, Proceedings of the National Academy of Sciences, vol.22, issue.22, pp.15508-15513, 2007. ,
DOI : 10.1093/nar/22.22.4673
URL : http://www.pnas.org/content/104/39/15508.full.pdf
Type VI secretion apparatus and phage tail-associated 282 protein complexes share a common evolutionary origin, Proc Natl Acad Sci U S A, vol.283, issue.106, pp.4154-4159, 2009. ,
VipB tubules by ClpV-mediated threading is crucial for type VI protein 286 secretion, EMBO J, vol.28, pp.315-325, 2009. ,
ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion, Molecular Microbiology, vol.6, issue.5, pp.1013-1028, 2013. ,
DOI : 10.1371/journal.pone.0023876
URL : http://onlinelibrary.wiley.com/doi/10.1111/mmi.12147/pdf
Type VI secretion requires a dynamic contractile phage tail-like structure, Nature, vol.1, issue.7388, pp.182-292, 2012. ,
DOI : 10.1038/nprot.2006.432
URL : http://europepmc.org/articles/pmc3527127?pdf=render
Type 6 secretion dynamics within and between bacterial cells. 294 Science, pp.815-295, 2012. ,
DOI : 10.1126/science.1222901
URL : http://europepmc.org/articles/pmc3557511?pdf=render
Imaging Type VI Secretion-Mediated Bacterial Killing, Cell Reports, vol.3, issue.1, pp.36-41, 2013. ,
DOI : 10.1016/j.celrep.2012.11.027
URL : https://hal.archives-ouvertes.fr/hal-01458227
VgrG, Tae, Tle, and beyond: the versatile arsenal of Type VI secretion effectors, Trends in Microbiology, vol.22, issue.9, pp.498-299, 2014. ,
DOI : 10.1016/j.tim.2014.06.004
URL : https://hal.archives-ouvertes.fr/hal-01458195
Type VI secretion system effectors: poisons with a purpose, Nature Reviews Microbiology, vol.8, issue.2, pp.137-148, 2014. ,
DOI : 10.1371/journal.pone.0057609
Structural biology of type VI secretion systems, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.364, issue.2, pp.1102-1111, 2012. ,
DOI : 10.1016/j.jmb.2006.08.078
URL : https://hal.archives-ouvertes.fr/hal-01458261
Structural characterization and oligomerization of the TssL protein, a 306 component shared by bacterial type VI and type IVb secretion systems, J Biol, vol.307, issue.287, pp.14157-14168, 2012. ,
Towards a Structural Comprehension of Bacterial Type VI Secretion Systems: Characterization of the TssJ-TssM Complex of an Escherichia coli Pathovar, PLoS Pathogens, vol.15, issue.11, pp.1002386-312, 2011. ,
DOI : 10.1371/journal.ppat.1002386.s010
URL : https://hal.archives-ouvertes.fr/hal-01458272
The SciZ protein anchors 313 the enteroaggregative Escherichia coli Type VI secretion system to the cell wall, p.314 ,
Anchoring the type VI secretion system to the 316 peptidoglycan, pp.535-540, 2010. ,
Structure???Function Analysis of the TssL Cytoplasmic Domain Reveals a New Interaction between the Type VI Secretion Baseplate and Membrane Complexes, Journal of Molecular Biology, vol.428, issue.22, pp.4413-4423, 2016. ,
DOI : 10.1016/j.jmb.2016.08.030
URL : https://hal.archives-ouvertes.fr/hal-01439100
Biogenesis and structure of a type 323 VI secretion membrane core complex, Nature, vol.523, pp.555-560, 2015. ,
Structure of the T4 baseplate and its function in triggering sheath contraction, Nature, vol.372, issue.7603, pp.346-352, 2016. ,
DOI : 10.1016/j.jmb.2007.05.022
Priming and polymerization of a bacterial contractile 329 tail structure, Nature, vol.531, pp.59-63, 2016. ,
Crystal structure of 334 secretory protein Hcp3 from Pseudomonas aeruginosa, J Struct Funct Genomics, vol.335, issue.12, pp.201121-201147 ,
Cambillau 337 C: Crystal structure and self-interaction of the type VI secretion tail-tube protein 338 from enteroaggregative Escherichia coli-repeat 340 proteins sharpen and diversify the type VI secretion system spike, PLoS One Nature, vol.2014, issue.500, pp.350-353, 2013. ,
VI secretion complex suggests a contraction-state-specific recycling 344 mechanism 345 **25 Atomic structure of T6SS 346 reveals interlaced array essential to function, Cell Rep Cell Kudryashev M, vol.8, issue.160, pp.20-30940, 2014. ,
Structure of the type VI secretion system 349 contractile sheath, Cell, vol.160, pp.952-962, 2015. ,
Structure and specificity of the Type VI secretion system 352 ,
In vivo structures of an intact type 355 VI secretion system revealed by electron cryotomography, EMBO Rep, vol.356, issue.18, pp.1090-1099, 2017. ,
CryoEM structure of the extended Type VI 359 secretion system tube-sheath complex, Nat Microbiol, p.360, 2017. ,
Contractile tail machines of bacteriophages Adv Exp Med 361, Biol, vol.2012, issue.726, pp.93-114 ,
Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems, Proceedings of the National Academy of Sciences, vol.113, issue.36, pp.10174-10179 ,
DOI : 10.1073/pnas.91.6.2146
Journet 366 L: TssK is a trimeric cytoplasmic protein interacting with components of both 367 ,
a core component of the bacterial Type VI secretion system, reveals 371 distinct oligomeric states of TssK and identifies a TssK-TssFG sub-complex, p.372 ,
1042/BJ20131426. 373 *34, Biochem J, vol.10, 2014. ,
Phage-Like Baseplate Is Recruited to the TssJLM Membrane 375 Complex via Multiple Contacts and Serves As Assembly Platform for Tail 376 ,
Camelid nanobodies: killing two birds with one stone, Current Opinion in Structural Biology, vol.32, p.380, 2015. ,
DOI : 10.1016/j.sbi.2015.01.001
URL : https://hal.archives-ouvertes.fr/hal-01439032
Type VI secretion TssK 381 baseplate protein exhibits structural similarity with phage receptor-binding 382 proteins and evolved to bind the membrane complex, Nat Microbiol, pp.383-385, 2017. ,
HsiE1 distinguishes type VI secretion classes, J Biol Chem, vol.289, pp.33032-387, 2014. ,
Type VI secretion systems of human gut Bacteroidales segregate into three genetic architectures, two of which are contained on mobile genetic elements, BMC Genomics, vol.110, issue.17, pp.58-391, 2016. ,
DOI : 10.1073/pnas.1300627110
Structure of lactococcal phage p2 396 baseplate and its mechanism of activation, Proc Natl Acad Sci, vol.397, issue.107, pp.6852-6857, 2010. ,